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Yorodumi- PDB-5tmc: Re-refinement of Thermus thermopiles DNA-directed RNA polymerase ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5tmc | ||||||
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Title | Re-refinement of Thermus thermopiles DNA-directed RNA polymerase structure | ||||||
Components |
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Keywords | TRANSFERASE / Symmetry Downshifting / Validation of Symmetry | ||||||
Function / homology | Function and homology information sigma factor activity / DNA-directed RNA polymerase complex / DNA-templated transcription initiation / ribonucleoside binding / DNA-directed 5'-3' RNA polymerase activity / DNA-directed RNA polymerase / protein dimerization activity / DNA-templated transcription / magnesium ion binding / DNA binding ...sigma factor activity / DNA-directed RNA polymerase complex / DNA-templated transcription initiation / ribonucleoside binding / DNA-directed 5'-3' RNA polymerase activity / DNA-directed RNA polymerase / protein dimerization activity / DNA-templated transcription / magnesium ion binding / DNA binding / zinc ion binding / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | Thermus thermophilus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.71 Å | ||||||
Authors | Wang, J. | ||||||
Citation | Journal: Cell(Cambridge,Mass.) / Year: 2004 Title: Structural basis for transcription regulation by alarmone ppGpp. Authors: Artsimovitch, I. / Patlan, V. / Sekine, S. / Vassylyeva, M.N. / Hosaka, T. / Ochi, K. / Yokoyama, S. / Vassylyev, D.G. | ||||||
History |
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Remark 0 | THIS ENTRY 5TMC REFLECTS AN ALTERNATIVE MODELING OF THE STRUCTURAL DATA IN R1SMYSF ORIGINAL DATA ...THIS ENTRY 5TMC REFLECTS AN ALTERNATIVE MODELING OF THE STRUCTURAL DATA IN R1SMYSF ORIGINAL DATA DETERMINED BY AUTHOR: I.ARTSIMOVITCH,V.PATLAN,S.SEKINE,M.N.VASSYLYEVA,T.HOSAKA, K.OCHI,S.YOKOYAMA,D.G.VASSYLYEV,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI). |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5tmc.cif.gz | 1.4 MB | Display | PDBx/mmCIF format |
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PDB format | pdb5tmc.ent.gz | 1.2 MB | Display | PDB format |
PDBx/mmJSON format | 5tmc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tm/5tmc ftp://data.pdbj.org/pub/pdb/validation_reports/tm/5tmc | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
-DNA-directed RNA polymerase subunit ... , 4 types, 5 molecules ABCDE
#1: Protein | Mass: 35056.164 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) References: UniProt: Q9Z9H6, UniProt: Q5SHR6*PLUS, DNA-directed RNA polymerase #2: Protein | | Mass: 125436.539 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / References: UniProt: Q8RQE9, DNA-directed RNA polymerase #3: Protein | | Mass: 170997.391 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / References: UniProt: Q8RQE8, DNA-directed RNA polymerase #4: Protein | | Mass: 11521.221 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) References: UniProt: Q72ID6, UniProt: Q8RQE7*PLUS, DNA-directed RNA polymerase |
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-Protein / Protein/peptide , 2 types, 2 molecules FZ
#5: Protein | Mass: 48568.008 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / References: UniProt: Q72L95, UniProt: Q5SKW1*PLUS |
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#6: Protein/peptide | Mass: 4103.049 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) |
-Non-polymers , 5 types, 155 molecules
#7: Chemical | ChemComp-PO4 / | ||||||
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#8: Chemical | ChemComp-MG / #9: Chemical | #10: Chemical | ChemComp-G4P / | #11: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 4.71 Å3/Da / Density % sol: 73.87 % / Description: AUTHOR USED THE SF DATA FROM ENTRY 1SMY. |
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-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||
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Reflection twin |
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-Processing
Software | Name: REFMAC / Version: 5.5.0109 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 2.71→48.51 Å / Cor.coef. Fo:Fc: 0.893 / Cor.coef. Fo:Fc free: 0.87 / Cross valid method: THROUGHOUT / ESU R: 0.091 / ESU R Free: 0.064 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. L-test and other twinning statistical tests have shown that the 1SMY data were partially twinned, but not perfectly twinned. With partial ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. L-test and other twinning statistical tests have shown that the 1SMY data were partially twinned, but not perfectly twinned. With partial twinning, the symmetry is partially upshifted to P6(5)22 from P6(5), which is consistent with the observed systematic absences and intensity merging R-factors reported for them. If the correct space group were P3(2), an up-shifted symmetry by a different twinning operation along the 3-fold axis could only generate P6(4), but not P6(5) because P3(2) is not a subgroup of P6(5). Moreover, the conversion of P3(2) to P6(5) using a perfect twinning method is not consistent with the L-test results, either, which suggests only a partial twinning, not perfect twinning. Given the problem of partial twinning in the data, model refinement was indeed very challenging. Six independent attempts of model refinement were made after proper crystallographic origin shift, starting with six different partial models according to the notes in author's notebook. All appear to have converged to similar crystallographic R-factor and free R-factor, even though the number of atoms in the final coordinates varied slightly among them. At the time of submission of this entry, the files for two of the six attempts have been located, but the remaining four files have not. It appears that there might be a mix-up in number of atoms among these files when reporting the number of atoms and R-factors.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 121.351 Å2
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Refinement step | Cycle: 1 / Resolution: 2.71→48.51 Å
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